Conggang Li

The paper uses high-resolution NMR spectroscopy to study protein interactions and modifications within intact mitochondria, providing insights into mitochondrial protein function and stability.

This study determines the high-resolution NMR structures of Apt38, a truncated variant of the serotonin-binding aptamer, revealing its G-quadruplex-duplex hybrid structure and serotonin binding mechanism.

This paper introduces two novel 19F NMR probes to study tyrosine ring-flip dynamics in proteins, showing they can quantify and modulate these motions in vitro and in living cells.

This paper introduces a method to produce 15N-labeled ssDNA for NMR studies of G-quadruplexes in cell lysates, revealing distinct ligand-binding behaviors in different environments.